Ligand Leu-Val
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Basic Ligand Information
Molecular Structure
C11H22N2O3
Leu-Val
MDSUKZSLOATHMH-IUCAKERBSA-N
L-Leu-L-Val, L-Leu-L-Val[side 2]
Roles as Enzyme Ligand
Substrate in Enzyme-catalyzed Reactions (3 results)
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Leu-Val + H2O = Leu + Val
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Leu-Val + H2O = Leu + Val
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L-Leu-L-Val + H2O = Leu + Val
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Product in Enzyme-catalyzed Reactions (3 results)
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FVNQHLCGSHLV + H2O = FVNQHLCGSH + L-Leu-L-Val + L-Val
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FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O = FVNQHLCGSHLVEA + Leu-Val + LVCGERGF + FYTPKA
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ATP + H2O + L-Leu-L-Val-[dipeptide-binding protein][side 1] = ADP + phosphate + L-Leu-L-Val[side 2] + [dipeptide-binding protein][side 1]
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Enzyme Kinetic Parameters
kcat Value (Turnover Number) (1 result)
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KM Value (3 results)
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References & Links
Literature References (5)
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Leucine aminopeptidase and other N-terminal exopeptidases
1971
Delange, R.J.; Smith, E.L.
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbäck, K. , eds. )
3
81-118
Aeromonas aminopeptidase
1976
Prescott, J.M.; Wilkes, S.H.
Methods Enzymol.
45
530-543
Specificity of Aeromonas aminopeptidase toward amino acid amides and dipeptides
1972
Wagner, F.W.; Wilkes, S.H.; Prescott, J.M.
J. Biol. Chem.
247
1208-1210
The purification and properties of an amidohydrolase from soybean
1974
Hoagland, R.E.; Graf, G.
Can. J. Biochem.
52
903-910
Specificity of the wound-induced leucine aminopeptidase (LAP-A) of tomato. Activity on dipeptide and tripeptide substrates
2000
Gu, Y.Q.; Walling, L.L.
Eur. J. Biochem.
267
1178-1187
Links to other databases for Leu-Val
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